YHR013C - Revision history

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001055 YHR013C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001055 YHR013C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''ARD1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr VIII:131440..130724
+|nowrap| Chr VIII:131446..130730
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000001055

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YHR013C:''' Subunit of N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); acetylates many proteins and thus affects telomeric silencing, cell cycle, heat-shock resistance, mating, and sporulation; human Ard1p levels are elevated in cancer cells<ref name='S000042046'>Park EC and Szostak JW (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J 11(6):2087-93 {{SGDpaper|S000042046}} PMID 1600941</ref><ref name='S000044111'>Mullen JR, et al. (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J 8(7):2067-75 {{SGDpaper|S000044111}} PMID 2551674</ref><ref name='S000073836'>Polevoda B and Sherman F (2003) Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem Biophys Res Commun 308(1):1-11 {{SGDpaper|S000073836}} PMID 12890471</ref><ref name='S000074487'>Gautschi M, et al. (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23(20):7403-14 {{SGDpaper|S000074487}} PMID 14517307</ref><ref name='S000129704'>Yu M, et al. (2009) Immunohistochemical analysis of human arrest-defective-1 expressed in cancers in vivo. Oncol Rep 21(4):909-15
+'''Description of YHR013C:''' Subunit of N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); acetylates many proteins and thus affects telomeric silencing, cell cycle, heat-shock resistance, mating, and sporulation; human Ard1p levels are elevated in cancer cells<ref name='S000074487'>Gautschi M, et al. (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23(20):7403-14 {{SGDpaper|S000074487}} PMID 14517307</ref><ref name='S000044111'>Mullen JR, et al. (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J 8(7):2067-75 {{SGDpaper|S000044111}} PMID 2551674</ref><ref name='S000042046'>Park EC and Szostak JW (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J 11(6):2087-93 {{SGDpaper|S000042046}} PMID 1600941</ref><ref name='S000073836'>Polevoda B and Sherman F (2003) Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem Biophys Res Commun 308(1):1-11 {{SGDpaper|S000073836}} PMID 12890471</ref><ref name='S000129704'>Yu M, et al. (2009) Immunohistochemical analysis of human arrest-defective-1 expressed in cancers in vivo. Oncol Rep 21(4):909-15
   {{SGDpaper|S000129704}} PMID 19287988</ref>
 <br>

@@ Line 8: / Line 8: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''ARD1 ''
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||'' ''
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''NAA10''
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YHR013C:''' Subunit of N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); acetylates many proteins and thus affects telomeric silencing, cell cycle, heat-shock resistance, mating, and sporulation; human Ard1p levels are elevated in cancer cells<ref name='S000129704'>Yu M, et al. (2009) Immunohistochemical analysis of human arrest-defective-1 expressed in cancers in vivo. Oncol Rep 21(4):909-15 {{SGDpaper|S000129704}} PMID 19287988</ref><ref name='S000074487'>Gautschi M, et al. (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23(20):7403-14 {{SGDpaper|S000074487}} PMID 14517307</ref><ref name='S000073836'>Polevoda B and Sherman F (2003) Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem Biophys Res Commun 308(1):1-11 {{SGDpaper|S000073836}} PMID 12890471</ref><ref name='S000044111'>Mullen JR, et al. (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J 8(7):2067-75 {{SGDpaper|S000044111}} PMID 2551674</ref><ref name='S000042046'>Park EC and Szostak JW (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J 11(6):2087-93
+'''Description of YHR013C:''' Subunit of N-terminal acetyltransferase NatA (Nat1p, Ard1p, Nat5p); acetylates many proteins and thus affects telomeric silencing, cell cycle, heat-shock resistance, mating, and sporulation; human Ard1p levels are elevated in cancer cells<ref name='S000042046'>Park EC and Szostak JW (1992) ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J 11(6):2087-93 {{SGDpaper|S000042046}} PMID 1600941</ref><ref name='S000044111'>Mullen JR, et al. (1989) Identification and characterization of genes and mutants for an N-terminal acetyltransferase from yeast. EMBO J 8(7):2067-75 {{SGDpaper|S000044111}} PMID 2551674</ref><ref name='S000073836'>Polevoda B and Sherman F (2003) Composition and function of the eukaryotic N-terminal acetyltransferase subunits. Biochem Biophys Res Commun 308(1):1-11 {{SGDpaper|S000073836}} PMID 12890471</ref><ref name='S000074487'>Gautschi M, et al. (2003) The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol 23(20):7403-14 {{SGDpaper|S000074487}} PMID 14517307</ref><ref name='S000129704'>Yu M, et al. (2009) Immunohistochemical analysis of human arrest-defective-1 expressed in cancers in vivo. Oncol Rep 21(4):909-15
-  {{SGDpaper|S000042046}} PMID 1600941</ref>
+  {{SGDpaper|S000129704}} PMID 19287988</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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	{{ShortCenteredHR}}		{{ShortCenteredHR}}
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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		+	Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
		+	<ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur.
		+	J Biol Chem 278(5):3265-74</ref>
		+	-->

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